ID H8Z3Y9_9GAMM Unreviewed; 1032 AA.
AC H8Z3Y9;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE Short=R protein {ECO:0000256|RuleBase:RU364115};
DE EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
GN ORFNames=Thi970DRAFT_04830 {ECO:0000313|EMBL:EIC21141.1};
OS Thiorhodovibrio frisius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodovibrio.
OX NCBI_TaxID=631362 {ECO:0000313|EMBL:EIC21141.1, ECO:0000313|Proteomes:UP000002964};
RN [1] {ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Overmann J.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EIC21141.1, ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|EMBL:EIC21141.1,
RC ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA Overmann J., Frigaard N.-U., Bryant D., Woyke T.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC fragments with terminal 5'-phosphates, ATP is simultaneously
CC hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000256|ARBA:ARBA00000851,
CC ECO:0000256|RuleBase:RU364115};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S. {ECO:0000256|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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DR EMBL; JH603170; EIC21141.1; -; Genomic_DNA.
DR RefSeq; WP_009151544.1; NZ_JH603170.1.
DR AlphaFoldDB; H8Z3Y9; -.
DR STRING; 631362.Thi970DRAFT_04830; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_6; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000002964; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd22332; HsdR_N; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 1.20.58.910; -; 1.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR004473; Restrct_endonuc_typeI_HsdR.
DR InterPro; IPR040980; SWI2_SNF2.
DR InterPro; IPR022625; TypeI_RM_Rsu_C.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF12008; EcoR124_C; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364115};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364115};
KW Reference proteome {ECO:0000313|Proteomes:UP000002964};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 261..442
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 485..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 117236 MW; ABEE02C4956C298D CRC64;
MSLTEQQLEQ KLIDTLVELK YSYRPDIRDK AALEANFRAK FEALNHVSLT DAEFARLRDS
LISADVFQAA KTLREIGYFQ REDGTPLHFM LVNLKDWCKN DFEVIHQLRI NTDSSHHRYD
VILLINGLPL VQIELKTLTI SPRRAMEQIV DYKHDPGNGY TNTLLCFMQL FIVSNRSNTY
YFANNHPQHF AFNAEERFLP IYQWADRDNR KITHLDDFAA AFLAKCTLGQ MLSRYMVLVA
SEQKLMIMRP YQIYAVQAIV DCIHQNRGNG FVWHTTGSGK TLTSFKASTL LKDNPDIEKC
LFVVDRKDLD RQTRIEFNKF QEGCVEENTN TETLVRRLLS EDYANKVIVT TIQKLGLALD
ETSKRAQQHR DQGKRTYKER LAPLRDKRLA IIFDECHRSQ FGDNHQAIKA FFPKAQLFGF
TGTPIFEENA SHTQIDGTVG RFKTTQDIFH SPLHAYTITH AIDDGNVLRF HIEYYKPEAK
AATADASADS DIAEPSTNAP AKTAKPKPER IHSQRAIAEA ILAKHDAATN QRRFNALLAT
ASINDAIAYY ELFKQLQAER QAPGGNESPD VRPLNIACVF SPPAEGNRDV KQLQEDLPQE
KADNQQEPEA KKAALRQILA DYNAHYGTNH SIGDFDGYYQ DVQQRIKDQQ YPNSDLPHRH
KIDLTIVVDM LLTGFDSKYL NTLYVDKNLK HHGLIQAFSR TNRVLNDTKP YGNILDFRAQ
ERAVDAAIAL FSGEDTSRSR EIWLVDPAPK VIEQLDTAVA QLEQFMAAQG QPCTPEAVNN
LKGDTARAGF IERFKDVQKL KNQLDQYTDL SDEQRAQVEQ RLPEDTHRSF KGMYLETAQR
LRDQQRQSGT GPDGGTPAPE VEQLEFEFVL FSSALIDYDY IMALIARYRQ EKPGKETLSR
DQIVSLLCGQ SNLMDERDEI IAYIDTLQAG KGHGGIEEIK GEYQVFKANK SRDELTAIAA
RHALAPEALH GFVEGILDRM IFDGEALTEL FAPLELGWKA RSQAETALMA ELTPVLKKQA
DGREISGLAA YE
//
